ID   GH109_STRFL             Reviewed;         494 AA.
AC   Q50EA3;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 1.
DT   03-AUG-2022, entry version 54.
DE   RecName: Full=Glycosyl hydrolase family 109 protein;
DE            EC=3.2.1.-;
DE   Flags: Precursor;
OS   Streptomyces filamentosus (Streptomyces roseosporus).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=67294;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NRRL 11379;
RX   PubMed=15870461; DOI=10.1099/mic.0.27757-0;
RA   Miao V., Coeffet-Legal M.F., Brian P., Brost R., Penn J., Whiting A.,
RA   Martin S., Ford R., Parr I., Bouchard M., Silva C.J., Wrigley S.K.,
RA   Baltz R.H.;
RT   "Daptomycin biosynthesis in Streptomyces roseosporus: cloning and analysis
RT   of the gene cluster and revision of peptide stereochemistry.";
RL   Microbiology 151:1507-1523(2005).
CC   -!- FUNCTION: Glycosidase. {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000250};
CC       Note=Binds 1 NAD(+) per subunit. The NAD(+) cannot dissociate.
CC       {ECO:0000250};
CC   -!- PTM: Predicted to be exported by the Tat system. The position of the
CC       signal peptide cleavage has not been experimentally proven.
CC   -!- SIMILARITY: Belongs to the Gfo/Idh/MocA family. Glycosyl hydrolase 109
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AY787762; AAX31528.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q50EA3; -.
DR   SMR; Q50EA3; -.
DR   GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR000683; Gfo/Idh/MocA-like_OxRdtase_N.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR006311; TAT_signal.
DR   Pfam; PF01408; GFO_IDH_MocA; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
KW   Glycosidase; Hydrolase; NAD; Signal.
FT   SIGNAL          1..58
FT                   /note="Tat-type signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT   CHAIN           59..494
FT                   /note="Glycosyl hydrolase family 109 protein"
FT                   /id="PRO_0000348566"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         104..105
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         126
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         175..178
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         195..196
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         224
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         253
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         272
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         284..287
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         284
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         366
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   494 AA;  54629 MW;  2266A58D88B8CE34 CRC64;
     MNDDARPAPE PQDIPPHSGA ADEVNRQDPS RRSVLWTTAG VAGAGLGLGA LGAGTASAAG
     RSAPDAVAAA EAVAAAPPRQ GRTMAGVPFE RRSTVRVGII GLGNRGDSMI DLFLALPGVQ
     VKAVCDTVRD KAEKAAKKVT AAGQPAPAIY AKDEHDYENL CKRGDIDFVY VVTPWELHFP
     MAKTAMLNGK HVGVECPIAM RLEELWQLVD LSERTRRHCM QLENCCYGKN EMRVLRMAHA
     GLFGELQHGA GAYNHDLREL MFDPDYYEGP WRRLWHTRLR GDLYPNHGFG PVANYMDVNR
     GDRVVSISSV GTTPLGLAAY REEHMPAGDP SWKESYIGAD RTISLVQTAK GRVIRLEHDV
     SSPHPYSRIN SLGGTKGVFE DYPERIYLEP TNTNHQWDDF KKYAEWDHWL WKEHANPPGG
     HGGMDYIMVF RLMQCMRLGL VPDFDVYDAA VWTAPVPLSH LSIKAKGVPL PIPDFTRGEW
     KKTRSGMDSE KPAE